Robert O. Fox

4.0k total citations · 1 hit paper
58 papers, 3.4k citations indexed

About

Robert O. Fox is a scholar working on Molecular Biology, Genetics and Materials Chemistry. According to data from OpenAlex, Robert O. Fox has authored 58 papers receiving a total of 3.4k indexed citations (citations by other indexed papers that have themselves been cited), including 48 papers in Molecular Biology, 16 papers in Genetics and 15 papers in Materials Chemistry. Recurrent topics in Robert O. Fox's work include RNA and protein synthesis mechanisms (21 papers), Protein Structure and Dynamics (17 papers) and Bacterial Genetics and Biotechnology (16 papers). Robert O. Fox is often cited by papers focused on RNA and protein synthesis mechanisms (21 papers), Protein Structure and Dynamics (17 papers) and Bacterial Genetics and Biotechnology (16 papers). Robert O. Fox collaborates with scholars based in United States, United Kingdom and Slovakia. Robert O. Fox's co-authors include Frederic M. Richards, Wendell A. Lim, Thomas R. Hynes, Roger A. Kautz, Philip A. Evans, Mario R. Ermácora, Michael S. Neuberger, Gareth T. Williams, Christopher M. Dobson and Marc Jacobs and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Robert O. Fox

58 papers receiving 3.3k citations

Hit Papers

A voltage-gated ion chann... 1982 2026 1996 2011 1982 200 400 600

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
Robert O. Fox 2.8k 707 436 379 364 58 3.4k
Michael Wittekind 2.4k 0.9× 581 0.8× 434 1.0× 411 1.1× 350 1.0× 42 3.4k
Rasmus H. Fogh 2.8k 1.0× 606 0.9× 355 0.8× 164 0.4× 450 1.2× 27 3.6k
Alain Chaffotte 2.1k 0.8× 605 0.9× 332 0.8× 661 1.7× 150 0.4× 67 3.1k
David E. Anderson 2.5k 0.9× 729 1.0× 530 1.2× 210 0.6× 244 0.7× 43 3.4k
Karyn T. O’Neil 3.6k 1.3× 726 1.0× 236 0.5× 829 2.2× 275 0.8× 53 4.4k
Jacob Anglister 2.4k 0.8× 458 0.6× 239 0.5× 766 2.0× 472 1.3× 89 3.3k
Francisco J. Blanco 4.9k 1.8× 1.3k 1.8× 447 1.0× 404 1.1× 645 1.8× 132 5.8k
L. Serrano 2.6k 0.9× 726 1.0× 337 0.8× 215 0.6× 194 0.5× 18 3.2k
R. Andrew Byrd 2.7k 1.0× 765 1.1× 288 0.7× 348 0.9× 1.1k 3.0× 109 4.1k
Claudio Vita 1.6k 0.6× 345 0.5× 277 0.6× 304 0.8× 169 0.5× 66 2.6k

Countries citing papers authored by Robert O. Fox

Since Specialization
Citations

This map shows the geographic impact of Robert O. Fox's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Robert O. Fox with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Robert O. Fox more than expected).

Fields of papers citing papers by Robert O. Fox

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert O. Fox. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Robert O. Fox. The network helps show where Robert O. Fox may publish in the future.

Co-authorship network of co-authors of Robert O. Fox

This figure shows the co-authorship network connecting the top 25 collaborators of Robert O. Fox. A scholar is included among the top collaborators of Robert O. Fox based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Robert O. Fox. Robert O. Fox is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Whitten, Steven T., et al.. (2008). Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM‐5 SH3 domain. Protein Science. 17(7). 1200–1211. 19 indexed citations
2.
Zhao, Yonghong, et al.. (2006). The crystal structure of the E. coli stress protein YciF. Protein Science. 15(11). 2605–2611. 22 indexed citations
3.
Schultz, David, Alan M. Friedman, Mark A. White, & Robert O. Fox. (2005). The crystal structure of the cis‐proline to glycine variant (P114G) of ribonuclease A. Protein Science. 14(11). 2862–2870. 12 indexed citations
4.
White, Mark A., et al.. (2003). Crystallization and preliminary X-ray diffraction analysis of Langat virus envelope protein domain III. Acta Crystallographica Section D Biological Crystallography. 59(6). 1049–1051. 11 indexed citations
5.
Friesen, Robert H., et al.. (2001). Structural and Functional Linkages Between Subunit Interfaces in Mammalian Pyruvate Kinase. Journal of Molecular Biology. 312(3). 525–540. 45 indexed citations
6.
Biswas, Roopa, et al.. (2000). Mapping RNA-protein interactions in ribonuclease P from Escherichia coli using disulfide-linked EDTA-fe 1 1Edited by K. Nagai. Journal of Molecular Biology. 296(1). 19–31. 45 indexed citations
7.
Richards, Frederic M., Richard Wynn, P.C. Harkins, & Robert O. Fox. (1997). Comparison of straight chain and cyclic unnatural amino acids embedded in the core of staphylococcal nuclease. Protein Science. 6(8). 1621–1626. 13 indexed citations
8.
Hodel, A.E., Robert O. Fox, & Roger A. Kautz. (1995). Stabilization of a strained protein loop conformation through protein engineering. Protein Science. 4(3). 484–495. 12 indexed citations
9.
Wynn, Richard, Cort L. Anderson, Frederic M. Richards, & Robert O. Fox. (1995). Interactions in nonnative and truncated forms of staphylococcal nuclease as indicated by mutational free energy changes. Protein Science. 4(9). 1815–1823. 9 indexed citations
10.
Kálmán, Franka, Stacey Ma, A.E. Hodel, Robert O. Fox, & Csaba Horváth. (1995). Charge and size effects in the capillary zone electrophoresis of nuclease A and its variants. Electrophoresis. 16(1). 595–603. 8 indexed citations
11.
Lim, Wendell A., Frederic M. Richards, & Robert O. Fox. (1994). Structural determinants of peptide-binding orientation and of sequence specificity in SH3 domains. Nature. 372(6504). 375–379. 445 indexed citations
12.
Ermácora, Mario R., et al.. (1994). Mapping Staphylococcal Nuclease Conformation Using an EDTA-Fe Derivative Attached to Genetically Engineered Cysteine Residues. Biochemistry. 33(46). 13625–13641. 37 indexed citations
13.
Hynes, Thomas R., A.E. Hodel, & Robert O. Fox. (1994). Engineering Alternative .beta.-Turn Types in Staphylococcal Nuclease. Biochemistry. 33(17). 5021–5030. 20 indexed citations
14.
Hodel, A.E., Roger A. Kautz, David M. Adelman, & Robert O. Fox. (1994). The importance of anchorage in determining a strained protein loop conformation. Protein Science. 3(4). 549–556. 14 indexed citations
15.
Ermácora, Mario R., et al.. (1993). Oxidative polypeptide cleavage mediated by EDTA-iron covalently linked to cysteine residues. Biochemistry. 32(47). 12761–12767. 68 indexed citations
16.
Kautz, Roger A. & Robert O. Fox. (1993). NMR analysis of staphylococcal nuclease thermal quench refolding kinetics. Protein Science. 2(5). 851–858. 18 indexed citations
17.
Sanders, S K, Robert O. Fox, & Paula Kavathas. (1991). Mutations in CD8 that affect interactions with HLA class I and monoclonal anti-CD8 antibodies.. The Journal of Experimental Medicine. 174(2). 371–379. 58 indexed citations
18.
Hynes, Thomas R. & Robert O. Fox. (1991). The crystal structure of staphylococcal nuclease refined at 1.7 Å resolution. Proteins Structure Function and Bioinformatics. 10(2). 92–105. 229 indexed citations
19.
Eftink, Maurice R., Camillo A. Ghiron, Roger A. Kautz, & Robert O. Fox. (1989). Fluorescence lifetime studies with staphylococcal nuclease and its site-directed mutant. Test of the hypothesis that proline isomerism is the basis for nonexponential decays. Biophysical Journal. 55(3). 575–579. 22 indexed citations
20.
Fox, Robert O., Philip A. Evans, & Christopher M. Dobson. (1986). Multiple conformations of a protein demonstrated by magnetization transfer NMR spectroscopy. Nature. 320(6058). 192–194. 94 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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